I u,fdireg n-YceyX-gil si lcncleityha edricoedsn a rypimar“ iaonm icda eutrstucr of a pit”onre enics eth dionitnfei of a amPyrir ueuttrrcs of a ptienor is “a enirla aihcn of imano .csi”da fI yuo essm htiw hte ayPmirr uetsru,crt as in eht equisnot ste,m uyo notacn form het nrSycaedo rscturuet fo eht ,rteinop wihch is dirmtnedee by teh nggbinoydd-nrheo ihcwh uocscr tbeeewn hte tpeepdi econbkab, nideepntned of hte R po.gurs I oehp ihts adme snsee.
Fmor iepiikdaw: oanr“Seydc trseucrut si loymfalr dndeefi yb teh ertnpat of yondhegr dbnos beneetw hte aomni dhgenroy nda obraxcly goexny osmta ni eht pteiped ebkabnco.” apsme(ihs ein)m
From Molecular Biology of the Cell:
Biologists distinguish four levels of organization in the structure of a protein. The amino acid sequence is known as the primary structure of the protein. Stretches of polypeptide chain that form α helices and β sheets constitute the protein’s secondary structure. The full three-dimensional organization of a polypeptide chain is sometimes referred to as the protein’s tertiary structure, and if a particular protein molecule is formed as a complex of more than one polypeptide chain, the complete structure is designated as the quaternary structure.
ok guys dan i oqeut morf msobtssehiteee/entd/t2hoa.piipwl:ceflr.ecta0/soowrpot-//grsmw4usti1c
0"9% ahev na eilfaiiedntb tineegc tuimoatn CL
O 1A1 dan CLO A21
cs
aues rbalamno eagclnol rinkginlc-sso aiv a elyicng ntitosutbisu ni hte oenaclrplog mceeoull "
chiwh masen that IO ahs a nliecyg sbtuittuonsi adn reoherft ist nauleb ot ofrm a doaysenrc rutsreutcu.
Deu ot cgel'inys llsam iezs, ti eerscta k"n"sik in het anomi caid seuenec.q These nkksi rae dndeee to ytccroelr form eht ysrndcoae rsuuctte.r
hteOr waersn:s
GyY--Xl si bckaoben rfo lgoeancl apahl .cnhai 3 clloagne ahpal sincah lrsipa to ormf lteipr hxl.ei iecGyln ahs no R ,rogpu anglwilo for ilblfeitixy nda omnofrati of etplri .hixel No gnlyeic erntevsp htis onnuutoics lpna,sirgi nnetprveig eth oimroatnf fo eaoncgll ndycroeas rrcutetus.
llceaR that ialaescelh-hp and -hbettsasee rea exeslamp fo scyerdnoa .tecurursst hiTs acn eb htotghu fo a nneoaaitmsitf fo eht paahl .hxlie
hrtNeoA awy to etg at ti is iav to:aminienil
A. yngoherd dobnnig tdlnouw ralley eagnhc sienc neherit leinaan onr yciegln era rlaoB.p lyG ;> alA hdul'nost ncgahe owh peloirn si dmidofei (I amen it OCDL,U if hetre was a sertci ehcdnnair ro hog,msinte but not a ergta sare.wD)n igonnth ot cieditan ttah lclnoega idndeogarte si terdlae in eporsnse to na AA bnsiusttot.iu ,sloA in eth oetcxnt of IO hhic(w si teh isnetpgern nt)o,mailpc ew ledaayr okwn htta hte mbrpole endsot' haev ahgytnin to do whit ginodr,teead mreo twhi hte nchgea ni ueuo.ctcErfu/ rinntts soHnlety on'td wnko.
sreHe’ oen yaw to leo-ifmeernso-ipsatc rscdedea“e yrgn-oodnbehd o”tafnm:ori ’Im ont a gbi naf of isht ilne fo oinsnar,ge tub tnlchcialey aalnnie as a dsei orpug ahs roem yhnde*srog fro tlantopie hyrnoged inobgnd than nylgcie:
nali:ean C3—H
gn:eycli H—
,oS ha“elycci,tn”l laanine owdlu pmeitr omre yngrohdbde-no motrnfoi,a chhwi itmhg ollwa oyu ot ilianmete htta hc.ocie
hTta s,aid it messe lstamo sseplimiob to uerl uot htowiut( ryev ctencihla odnwgleek or meos divdoepr tnimaeexlrep a)atd atth eth yilsltgh ergalr inlnaea sode otn rimipa hygonedr idgnnob eeebntw elaognlc lumeolces iav rtcsei p(ltsia)a etinnefeer.cr In leirpsm rmtes, cnies nelnaia si ae,rglr ouy lwduo thikn ttah ti umst ehoomws rnfteriee wiht eth bio-ryhoegndnndg ahtt usrocc tiwh hte tw-idplye glnycei.
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trtlyi*cS ke,igapsn s’ti ton eth bmneur fo ydsrheong btu asol eht esgtthnr of the ilopde that sieflttciaa dyneorhg obnd:ign a drgoneyh bondu ot a rgolsytn netveeoraeitclg ceumolle kile runofeil wlli a”pae“pr eorm sopvtiei a,nd utsh, -ghorbndnydeo omre grslonty iwht a rabeyn oygnxe (rmpaocde wiht a ydoerghn dnetccoen ot bocran, ofr axpee.)lm
urFterh i:radeng
From Molecular Biology of the Cell:
Hydroxylysines and hydroxyprolines are infrequently found in other animal proteins, although hydroxyproline is abundant in some proteins in the plant cell wall. In collagen, the hydroxyl groups of these amino acids are thought to form interchain hydrogen bonds that help stabilize the triple-stranded helix. Conditions that prevent proline hydroxylation, such as a deficiency of ascorbic acid (vitamin C), have serious consequences. (Emphasis mine)
From Molecular Biology of the Cell:
The primary feature of a typical collagen molecule is its long, stiff, triple-stranded helical structure, in which three collagen polypeptide chains, called α chains, are wound around one another in a ropelike superhelix (Figure 19-43). Collagens are extremely rich in proline and glycine, both of which are important in the formation of the triple-stranded helix. Proline, because of its ring structure, stabilizes the helical conformation in each α chain, while glycine is regularly spaced at every third residue throughout the central region of the α chain. Being the smallest amino acid (having only a hydrogen atom as a side chain), glycine allows the three helical α chains to pack tightly together to form the final collagen superhelix (see Figure 19-43).
I ghimt be kigvoirhentn it btu, H odbn mfrtonoai of a'sa mesak teh ndarcyseo tsrecutru of eht iptrone laec(nglo ni ihts aecs). heT ylG ot alA tttbsousiuin edso stelur in sels H dnbo ,rtioanfom ubt of uvliniddai asa' tno between nogllaec umeleslco t(hat ihtgm be roem rfo rqytaueran etstrucur)
myiPrra ctetruurs = miaon adci dscqaecneSn uyeore eutsrruct = scetrturu refmdo wtih a lsgnei mnaio ciad eqcusene (etab plaedte htes,e alpah ,hxeil eryact) ertTi tsuuctrer = eulimtlp rndoaecys truusercst necgtiairtn eorehtgt (pulltiem baet laeedtp tesshe astcdek on otp of ceah hrte,o ntearQe yrurca)t etrurctus = reiotnp terrucstu fdermo orfm fdgolni fo all tyitrrea trtuusescr ot eamk bdngini essti, cet.
eciSn het iaaelnn swa upt in eapcl of the ,cnyiGel eth irpryma ruurtctse aws lnueba to romf na aaphl ehlxi icnes phlaa exihl ursecurstt ened a pliucrtaar cqeeusen (ylg - -x )y in ordre ot fomr ydegrnho bonsd ot eepk het xiehl et.slba
athw si lnagecol ? a esoncydar etnpior eustt.rucr
newh oyu everom cynl,gei het stmo aaudbtnn noima idac , mrof hte psruorcre oeumllec lwli you teg a prrpeo daesrocny rueucstrt ? NO
Gyl is poa,rl ielnaAn si nlnoraop and hohyoripdbc. sienessM csveavoernotnni muaont.ti sheeT sAA vahe ntrfeidfe lehccima espoirptre iwchh lead ot dspeiturd ntoeirp ilongdf saeyn(cdro cs)rrttuu.e liSmria ot Gul - aVl buottuiitsns ni lceikS leCl .esDasei
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$279$49I hitnk ti sah mionhetgs to od ihtw cylgien ud(e ot its amlls siez it can fti in anmy aplecs ewrhe tohre iomna dcsia nca otn nad heenc ti roeisvdp usurrctlat“ t”scosmpecan to eht ol,alnceg .ei. upt a nikk in teh hpala h.elxi) fI ylcngie si lscdaepim yb etnmghios ls,ee I on’dt tihkn pnl-cgoorale acn mofr sit rceroct oecarndsy c.rtesuutr
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